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Abstracts (poster) - Wissenschaft Online

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Peter Hemmerich, Stefanie Weidtkamp-Peters, Christian Hoischen, Lars Schmiedeberg,<br />

Indri Erliandri, Stephan Diekmann<br />

CENP-I as a new epigentic mark at centromere chromatin<br />

Epigenetic marking of a DNA locus may be realized by posttranslational modifications of<br />

nucleosomal histones or by stable binding of a specific protein at that locus. Centromere<br />

identity is believed to be conveyed by CENP-A, a specialized histone H3 analog that<br />

substitutes canonical H3 within centromeric nucleosomes. CENP-A is constitutively<br />

present at centromeres and required for the association of all other kinetochore proteins.<br />

To test whether these epigenetic properties are unique to CENP-A we have assessed the<br />

exchange rates of inner centromere proteins by quantitative microscopy throughout the<br />

cell cycle in living human cells (1). We demonstrate that, in addition to CENP-A, CENP-I<br />

is also a stable centromere component that does at no time exchange with soluble pools<br />

at centromeres. Loading of CENP-I onto centromeric chromatin occurs co-replicationally,<br />

while CENP-A is loaded in early G1. A subfraction of CENP-H (~20%) also stays stably<br />

bound to centromeres throughout the cell cyle. In contrast, CENP-B, CENP-C, and<br />

hMis12 turn over completely at centromeres with residence times ranging between<br />

seconds to hours. Our data reveal a wide range of cell cycle-specific assembly plasticity<br />

of the centromere during the cell-cycle and identify CENP-I as a potentially additional<br />

epigentic marker at centromeres.<br />

Literature<br />

(1) Hemmerich et al., J. Cell Biol. (2008) in press<br />

contact:<br />

PhD Peter Hemmerich<br />

Leibniz Institute for Age Research<br />

Fritz-Lipmann-Institute<br />

phemmer@fli-leibniz.de<br />

Beutenbergstr. 11<br />

07745 Jena (Germany)

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